Correlation among the proton charges and molecular masses of myosin subunits

• Published in: FEBS letters Vol. 249; no. 1; pp. 8 - 12
• Main Authors: Bechet, J-J, d'Albis, A
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 22.05.1989; Elsevier
• Subjects: A1LC, higher molecular mass alkali (or essential) light chain; A2LC, lower molecular mass alkali (or essential) light chain; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Chickens; Contractile proteins; Electrophoresis; Electrophoresis - methods; Fundamental and applied biological sciences. Psychology; Heavy chain; Holoproteins; Humans; Hydrogen-Ion Concentration; Isoelectric Point; Light chain; Mice; Molecular mass; Molecular Weight; Myosin; Myosin Subfragments; Myosins; Peptide Fragments; Proteins; Protons; Rabbits; Rats; RLC, regulatory light chain; Space life sciences; Species Specificity; Isoelectric point; Myosin; A1LC, higher molecular mass alkali (or essential) light chain; Electrophoresis; A2LC, lower molecular mass alkali (or essential) light chain; Molecular mass; Heavy chain; Light chain; RLC, regulatory light chain; heavy-»Peptide chain; Gel electrophoresis; light-Peptide chain; Contractile protein; Subunit; Physicochemical properties; Aminoacid sequence
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(89)80004-3

The molecular masses and isoelectric points of myosin light and heavy chains were calculated from their known primary sequences and their respective distribution in a two-dimensional graph is displayed. Implications for the electrophoretic study of myosin subunits are inferred from this analysis.